Journal
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
Volume 37, Issue 6, Pages 617-624Publisher
OXFORD UNIV PRESS
DOI: 10.1007/s10295-010-0709-6
Keywords
p-Coumaric acid; Ferulic acid; Phenolic acid decarboxylase; Phenolic acids; Vinyl phenol
Categories
Funding
- Comision Interministerial de Ciencia y Tecnologia [CSD2007-00063 FUN-C-FOOD, AGL2005-00470, AGL2008-01052]
- Instituto Nacional de Investigacion Agraria y Alimentaria [RM2008-00002]
- (ALIBIRD) (Comunidad de Madrid) [S-0505/AGR/000153, S2009/AGR-1469]
- I3P-CSIC
- FPI-MEC
- Ministerio de Ciencia e Innovacion
Ask authors/readers for more resources
Phenolic acid decarboxylase (PAD) catalyzes the synthesis of vinyl phenols from hydroxycinnamic acids. The gene encoding PAD from Lactobacillus brevis was cloned and expressed as a fusion protein in Escherichia coli. The recombinant PAD enzyme is a heat-labile enzyme that functions optimally at 22A degrees C and pH 6.0. The purified enzyme did not show thermostability at temperatures above 22A degrees C. L. brevis PAD is able to decarboxylate exclusively the hydroxycinnamic acids, such as p-coumaric, caffeic, and ferulic acids, with K (m) values of 0.98, 0.96, and 0.78 mM, respectively. The substrate specificity exhibited by L. brevis PAD is similar to the PAD isolated from Bacillus subtilis and B. pumilus, but different from that of L. plantarum and Pediococcus pentosaceus. As the C-terminal region may be involved in determining PAD substrate specificity and catalytic capacity, amino acid differences among these proteins could explain the differences observed. The substrate specificity shown by L. brevis PAD shows promise for the synthesis of high-added value products from plant wastes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available